Abstract
Fluorometry has been extensively employed in studies involving molecular complexes because of its exceptional sensitivity and time resolution. Molecular complexation is widespread in nature; indeed, it is through that process that biopolymers such as DNA and enzymes are assembled and carry out their functions. Covalent binding holds together strong complexes, while hydrogen-bonding, charge-transfer, electrostatic, and hydrophobic interactions are mainly responsible for the stability of weaker complexes. Some high-molecular-weight complexes contain fluorescent building blocks that report on their immediate environment; e.g., proteins contain tryptophan and tyrosine fluorescent amino acid residues. Other biomolecules may be labeled with fluorophores by forming noncovalent or covalent complexes. Time-resolved and time-integrated fluorometric investigations of these systems yield information pertaining to the following:
-
(a)
the polarity and fluidity of the microenvironment of the emitter,
-
(b)
the occurrence of structural fluctuations in the biomolecule within the time span of light emission,
-
(c)
the occurrence of excited-state time-dependent interactions between the emitter and the solvent or neighboring chemical groups of the biomolecule,
-
(d)
the overall shape and dimensions of the biomolecule,
-
(e)
and the exchange of excitation energy between the emitter and other components of the biomolecule.
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Georghiou, S. (1981). Fluorometric Studies of Biologically Important Molecular Complexes. In: Wehry, E.L. (eds) Modern Fluorescence Spectroscopy. Modern Analytical Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1092-1_5
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